Structure of PDB 2zp7 Chain D

Receptor sequence
>2zp7D (length=391) Species: 262724 (Thermus thermophilus HB27) [Search protein sequence]
SWSEAFGKGAGRIQASTIRELLKLTQRPGILSFAGGLPAPELFPKEEAAE
AAARILREKGEVALQYSPTEGYAPLRAFVAEWIGVRPEEVLITTGSQQAL
DLVGKVFLDEGSPVLLEAPSYMGAIQAFRLQGPRFLTVPAGEEGPDLDAL
EEVLKRERPRFLYLIPSFQNPTGGLTPLPARKRLLQMVMERGLVVVEDDA
YRELYFGEARLPSLFELAREAGYPGVIYLGSFSKVLSPGLRVAFAVAHPE
ALQKLVQAKQGADLHTPMLNQMLVHELLKEGFSERLERVRRVYREKAQAM
LHALDREVPKEVRYTRPKGGMFVWMELPKGLSAEGLFRRALEENVAFVPG
GPFFANGGGENTLRLSYATLDREGIAEGVRRLGRALKGLLA
3D structure
PDB2zp7 Mechanism for multiple-substrates recognition of alpha-aminoadipate aminotransferase from Thermus thermophilus
ChainD
Resolution2.26 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.6.1.39: 2-aminoadipate transaminase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 LEU D Y70 L268 Y66 L264
BS02 PLP D G99 S100 Q101 Y125 N174 D202 A204 Y205 S235 S237 K238 R245 G95 S96 Q97 Y121 N170 D198 A200 Y201 S231 S233 K234 R241
Gene Ontology
Molecular Function
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0047536 2-aminoadipate transaminase activity
Biological Process
GO:0009058 biosynthetic process
GO:0019878 lysine biosynthetic process via aminoadipic acid
GO:1901605 alpha-amino acid metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2zp7, PDBe:2zp7, PDBj:2zp7
PDBsum2zp7
PubMed18831049
UniProtQ72LL6|LYSN_THET2 2-aminoadipate transaminase (Gene Name=lysN)

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